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Database: UniProt/TrEMBL
Entry: B5YKQ3_THEYD
LinkDB: B5YKQ3_THEYD
Original site: B5YKQ3_THEYD 
ID   B5YKQ3_THEYD            Unreviewed;       192 AA.
AC   B5YKQ3;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   28-MAR-2018, entry version 55.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=THEYE_A0986 {ECO:0000313|EMBL:ACI20791.1};
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /
OS   YP87).
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae;
OC   Thermodesulfovibrio.
OX   NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI20791.1, ECO:0000313|Proteomes:UP000000718};
RN   [1] {ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii
RT   strain ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001147; ACI20791.1; -; Genomic_DNA.
DR   RefSeq; WP_012545523.1; NC_011296.1.
DR   RefSeq; YP_002248818.1; NC_011296.1.
DR   ProteinModelPortal; B5YKQ3; -.
DR   STRING; 289376.THEYE_A0986; -.
DR   EnsemblBacteria; ACI20791; ACI20791; THEYE_A0986.
DR   GeneID; 6943269; -.
DR   KEGG; tye:THEYE_A0986; -.
DR   PATRIC; fig|289376.4.peg.970; -.
DR   eggNOG; ENOG4107XIJ; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; B5YKQ3; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; TYEL289376:G1GCQ-985-MONOMER; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000718};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000718}.
FT   DOMAIN       15     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        25     25       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  22443 MW;  9F335CBA77401FC8 CRC64;
     MPYEAKDYSK LIGMPGFSET LLKNHFTLYQ GYVTNTNKVL EILETMLKEG KTTIPEYAEL
     KRRLGWEWNG VRLHEYYFEN LGGDGVFPKD GKLAKLINEN FGSFENWLKD FKATGTMRGI
     GWIILYQDIL SGKLINFWIN EHDVGHPAGC NPLLIMDVFE HAFMIDYGLK RADYIEAFFK
     NINWKEVEKR IR
//
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